To gain understanding of the role of Slc45a2 (show SLC45A2 Proteins) and its possible interactions with other proteins involved in melanization, the role of the V-ATPase (show ATP6V1H Proteins) as a melanosomal acidifier, was analyzed.

We report biallelic mutations in ATP6V1E1 (show ATP6V1E1 Proteins) and ATP6V1A, respectively encoding the E1 and A subunits of the V1 domain of V-ATPase (show ATP6V1H Proteins), as a cause of distinct metabolic and multisystemic cutis laxa entities.

preparations of Na+,K(+)-ATPase (show ATP1A1 Proteins) isozymes from calf brain that contain catalytic subunits of three types (alpha 1, alpha 2, and alpha 3) were obtained.The real isozyme composition of the Na+ pump from the grey matter and the brain stem was determined.

Protein Summary

This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c', and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This encoded protein is one of two V1 domain A subunit isoforms and is found in all tissues. Transcript variants derived from alternative polyadenylation exist.